ArticleMolecular & cellular proteomics : MCP2014
PepExplorer: a similarity-driven tool for analyzing de novo sequencing results.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- NovoLign: metaproteomics by sequence alignment.ISME communications · 2024Article
- Exploring the Sexual Dimorphism of Crustacean Neuropeptide Expression UsingJournal of proteome research · 2021Article
- Mass Spectrometry Quantification, Localization, and Discovery of Feeding-Related Neuropeptides inACS chemical neuroscience · 2021Article
- ProAlanase is an Effective Alternative to Trypsin for Proteomics Applications and Disulfide Bond Mapping.Molecular & cellular proteomics : MCP · 2020Article
- Flying blind, or just flying under the radar? The underappreciated power of de novo methods of mass spectrometric peptide identification.Protein science : a publication of the Protein Society · 2020Review
- Combination of Proteogenomics with PeptidemBio · 2019Article
- Data Independent Acquisition Mass Spectrometry Method for Improved Neuropeptidomic Coverage in Crustacean Neural Tissue Extracts.Analytical chemistry · 2019Article
- Article
- A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom.Scientific data · 2017Article
- Mass spectrometry-assisted gel-based proteomics in cancer biomarker discovery: approaches and application.Theranostics · 2017Review
- Article
- Integrated analysis of shotgun proteomic data with PatternLab for proteomics 4.0.Nature protocols · 2016Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Peptide spectrum matching is the current gold standard for protein identification via mass-spectrometry-based proteomics. Peptide spectrum matching compares experimental mass spectra against theoretical spectra generated from a protein sequence database to perform identification, but protein sequences not present in a database cannot be identified unless their sequences are in part conserved. The alternative approach, de novo sequencing, can make it possible to infer a peptide sequence directly from a mass spectrum, but interpreting long lists of peptide sequences resulting from large-scale experiments is not trivial. With this as motivation, PepExplorer was developed to use rigorous pattern recognition to assemble a list of homologue proteins using de novo sequencing data coupled to sequence alignment to allow biological interpretation of the data. PepExplorer can read the output of various widely adopted de novo sequencing tools and converge to a list of proteins with a global false-discovery rate. To this end, it employs a radial basis function neural network that considers precursor charge states, de novo sequencing scores, peptide lengths, and alignment scores to select similar protein candidates, from a target-decoy database, usually obtained from phylogenetically related species. Alignments are performed using a modified Smith-Waterman algorithm tailored for the task at hand. We verified the effectiveness of our approach using a reference set of identifications generated by ProLuCID when searching for Pyrococcus furiosus mass spectra on the corresponding NCBI RefSeq database. We then modified the sequence database by swapping amino acids until ProLuCID was no longer capable of identifying any proteins. By searching the mass spectra using PepExplorer on the modified database, we were able to recover most of the identifications at a 1% false-discovery rate. Finally, we employed PepExplorer to disclose a comprehensive proteomic assessment of the Bothrops jararaca plasma, a known biological source of natural inhibitors of snake toxins. PepExplorer is integrated into the PatternLab for Proteomics environment, which makes available various tools for downstream data analysis, including resources for quantitative and differential proteomics.
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Registered trials
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